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. 2021 Jul 8;12(7):685. doi: 10.1038/s41419-021-03950-y

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — A catRAPID fragment-based prediction assays of interaction between ZFP36 and CREBBP identified a strong interaction with high confidence levels (interaction propensity = 49 and discriminative power = 94%). B Western blotting analysis followed by RNA pull-downs, incubated with lysed lung epithelial-2 cell supernatant. GAPDH was used as a control. C Fold enrichment of CREBBP expression in RIP assays performed with ZFP36-coated beads. D, F Lung epithelial-2 cells underexpressing (D) or overexpressing (F) ZFP36 were stably transfected with luciferase constructs carrying the 3ʹUTR of the gene encoding CREBBP or empty vector (pGL3). Luciferase activities were measured and normalized to the activities obtained in pGL3-transfected cells (n = 3 in every group, **P < 0.01). E, G Remaining CREBBP mRNA levels were measured in lung epithelial-2 cells by real-time PCR (n = 3 in every group).